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Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution
Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution
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Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution

Bohn, Stefan ; Beck, Florian ; Sakata, Eri ; Walzthoeni, Thomas ; Beck, Martin ; Aebersold, Ruedi ; Förster, Friedrich ; Baumeister, Wolfgang ; Nickell, Stephan

Proceedings of the National Academy of Sciences - PNAS, 2010-12, Vol.107 (49), p.20992-20997 [Periódico revisado por pares]

United States: National Academy of Sciences

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2
In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment
In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment
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In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment

Guo, Qiang ; Lehmer, Carina ; Martínez-Sánchez, Antonio ; Rudack, Till ; Beck, Florian ; Hartmann, Hannelore ; Pérez-Berlanga, Manuela ; Frottin, Frédéric ; Hipp, Mark S. ; Hartl, F. Ulrich ; Edbauer, Dieter ; Baumeister, Wolfgang ; Fernández-Busnadiego, Rubén

Cell, 2018-02, Vol.172 (4), p.696-705.e12 [Periódico revisado por pares]

United States: Elsevier Inc

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3
Proteasomes tether to two distinct sites at the nuclear pore complex
Proteasomes tether to two distinct sites at the nuclear pore complex
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Proteasomes tether to two distinct sites at the nuclear pore complex

Albert, Sahradha ; Schaffer, Miroslava ; Beck, Florian ; Mosalaganti, Shyamal ; Asano, Shoh ; Thomas, Henry F. ; Plitzko, Jürgen M. ; Beck, Martin ; Baumeister, Wolfgang ; Engel, Benjamin D.

Proceedings of the National Academy of Sciences - PNAS, 2017-12, Vol.114 (52), p.13726-13731 [Periódico revisado por pares]

United States: National Academy of Sciences

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4
High-resolution structure and biophysical characterization of the nucleocapsid phosphoprotein dimerization domain from the Covid-19 severe acute respiratory syndrome coronavirus 2
High-resolution structure and biophysical characterization of the nucleocapsid phosphoprotein dimerization domain from the Covid-19 severe acute respiratory syndrome coronavirus 2
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High-resolution structure and biophysical characterization of the nucleocapsid phosphoprotein dimerization domain from the Covid-19 severe acute respiratory syndrome coronavirus 2

Zinzula, Luca ; Basquin, Jerome ; Bohn, Stefan ; Beck, Florian ; Klumpe, Sven ; Pfeifer, Günter ; Nagy, István ; Bracher, Andreas ; Hartl, F. Ulrich ; Baumeister, Wolfgang

Biochemical and biophysical research communications, 2021-01, Vol.538, p.54-62 [Periódico revisado por pares]

United States: Elsevier Inc

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5
Structure of the human 26S proteasome at a resolution of 3.9 Å
Structure of the human 26S proteasome at a resolution of 3.9 Å
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Structure of the human 26S proteasome at a resolution of 3.9 Å

Schweitzer, Andreas ; Aufderheide, Antje ; Rudack, Till ; Beck, Florian ; Pfeifer, Günter ; Plitzko, Jürgen M. ; Sakata, Eri ; Schulten, Klaus ; Förster, Friedrich ; Baumeister, Wolfgang

Proceedings of the National Academy of Sciences - PNAS, 2016-07, Vol.113 (28), p.7816-7821 [Periódico revisado por pares]

United States: National Academy of Sciences

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6
Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach
Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach
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Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach

Lasker, Keren ; Förster, Friedrich ; Bohn, Stefan ; Walzthoeni, Thomas ; Villa, Elizabeth ; Unverdorben, Pia ; Beck, Florian ; Aebersold, Ruedi ; Sali, Andrej ; Baumeister, Wolfgang

Proceedings of the National Academy of Sciences - PNAS, 2012-01, Vol.109 (5), p.1380-1387 [Periódico revisado por pares]

United States: National Academy of Sciences

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7
Structure of the 26S proteasome with ATP-γS bound provides insights into the mechanism of nucleotide-dependent substrate translocation
Structure of the 26S proteasome with ATP-γS bound provides insights into the mechanism of nucleotide-dependent substrate translocation
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Structure of the 26S proteasome with ATP-γS bound provides insights into the mechanism of nucleotide-dependent substrate translocation

Śledź, Paweł ; Unverdorben, Pia ; Beck, Florian ; Pfeifer, Günter ; Schweitzer, Andreas ; Förster, Friedrich ; Baumeister, Wolfgang

Proceedings of the National Academy of Sciences - PNAS, 2013-04, Vol.110 (18), p.7264-7269 [Periódico revisado por pares]

United States: National Academy of Sciences

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8
In situ architecture of the algal nuclear pore complex
In situ architecture of the algal nuclear pore complex
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In situ architecture of the algal nuclear pore complex

Mosalaganti, Shyamal ; Kosinski, Jan ; Albert, Sahradha ; Schaffer, Miroslava ; Strenkert, Daniela ; Salomé, Patrice A ; Merchant, Sabeeha S ; Plitzko, Jürgen M ; Baumeister, Wolfgang ; Engel, Benjamin D ; Beck, Martin

Nature communications, 2018-06, Vol.9 (1), p.2361-8, Article 2361 [Periódico revisado por pares]

England: Nature Publishing Group

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9
Near-atomic resolution structural model of the yeast 26S proteasome
Near-atomic resolution structural model of the yeast 26S proteasome
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Near-atomic resolution structural model of the yeast 26S proteasome

Beck, Florian ; Unverdorben, Pia ; Bohn, Stefan ; Schweitzer, Andreas ; Pfeifer, Günter ; Sakata, Eri ; Nickell, Stephan ; Plitzko, Jürgen M. ; Villa, Elizabeth ; Baumeister, Wolfgang ; Förster, Friedrich

Proceedings of the National Academy of Sciences - PNAS, 2012-09, Vol.109 (37), p.14870-14875 [Periódico revisado por pares]

United States: National Academy of Sciences

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10
The Architecture of Traveling Actin Waves Revealed by Cryo-Electron Tomography
The Architecture of Traveling Actin Waves Revealed by Cryo-Electron Tomography
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The Architecture of Traveling Actin Waves Revealed by Cryo-Electron Tomography

Jasnin, Marion ; Beck, Florian ; Ecke, Mary ; Fukuda, Yoshiyuki ; Martinez-Sanchez, Antonio ; Baumeister, Wolfgang ; Gerisch, Günther

Structure (London), 2019-08, Vol.27 (8), p.1211-1223.e5 [Periódico revisado por pares]

United States: Elsevier Ltd

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